Deep learning for intrinsically disordered proteins: From improved predictions to deciphering conformational ensembles

Curr Opin Struct Biol. 2024 Dec:89:102950. doi: 10.1016/j.sbi.2024.102950. Epub 2024 Nov 12.

Abstract

Intrinsically disordered proteins (IDPs) lack a stable three-dimensional structure under physiological conditions, challenging traditional structure-based prediction methods. This review explores how modern deep learning approaches, which have revolutionized structure prediction for globular proteins, have impacted protein disorder predictions. We highlight the role of community-driven efforts in curating data and assessing state-of-the-art, which have been crucial in advancing the field. We also review state-of-the-art methods utilizing deep learning techniques, highlighting innovative approaches. We also address advancements in characterizing protein conformational ensembles directly from sequence data using novel machine learning methods.

Publication types

  • Review

MeSH terms

  • Deep Learning*
  • Humans
  • Intrinsically Disordered Proteins* / chemistry
  • Intrinsically Disordered Proteins* / metabolism
  • Models, Molecular
  • Protein Conformation*

Substances

  • Intrinsically Disordered Proteins